Crystallization and preliminary data for the ferric form of Lucina pectinata hemoglobin I

Elena Casale, Claudia Lionetti, Alessandro Coda, Angelo Merli, Paolo Ascenzi, Jonathan B. Wittenberg, Martine Bolognesi

Research output: Contribution to journalArticlepeer-review


Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina pectinata has been crystallized in a form suitable for atomic resolution X-ray structural investigations. The crystals have been grown at pH 4.8, in 0.05 m-acetate buffer, using 2·6 m-ammonium sulfate as precipitating agent. The crystals belong to the monoclinic space group P21 with unit cell constants a = 500 A ̊, b = 38.6 A ̊, c = 42.1 A ̊, β = 107.1{ring operator}, and contain one molecule (14,000 Mr) in the asymmetric unit. By means of single crystal microspectrophotometry it has been shown that the crystals contain the ferric form of L. pectinata "sulfide reactive" hemoglobin I. On the other hand, by careful control of the buffering medium composition, it has been possible to obtain stable crystals of the deoxy, oxy and sulfide forms of the protein.

Original languageEnglish
Pages (from-to)447-449
Number of pages3
JournalJournal of Molecular Biology
Issue number3
Publication statusPublished - Dec 5 1991


  • hemoglobin crystals
  • Lucina pectinata Hb I
  • mollusc globin
  • monomeric globin
  • X-ray crystallography

ASJC Scopus subject areas

  • Virology


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